Ion Transport through Transmembrane Channels: Ab Initio Perspective

  • Jordan P
  • 1


    Mendeley users who have this article in their library.
  • 4


    Citations of this article.


The permeation of ions through channel proteins is influenced by many structural parameters. Among them are the composition of the bathing electrolytes, the structure of the water–membrane interface, the packing of the phospholipid, the folding of the channel protein, and the structure of the pore–water interface. There is uncertainty regarding both the structural and force field parameters needed to describe ionic interaction with channel-forming proteins. No single model calculation has included enough features of the real physical situation, even for a pore former as simple as gramicidin, to provide a definitive theoretical picture of selectivity. However, by comparing the results of calculations based on different reasonable models of the ion–water–gramicidin system, significant interpretive insights can be gained. As more structural proposals for describing the selectivity regions of physiologically important channel-forming proteins become available, ab initio methods can be used to construct permeation-free energy profiles and test various models. © 1988 Academic Press, Inc.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Peter C. Jordan

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free